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Deciphering the late steps of rifamycin biosynthesis

Author

Listed:
  • Feifei Qi

    (Chinese Academy of Sciences)

  • Chao Lei

    (Chinese Academy of Sciences)

  • Fengwei Li

    (Chinese Academy of Sciences)

  • Xingwang Zhang

    (Chinese Academy of Sciences)

  • Jin Wang

    (Chinese Academy of Sciences)

  • Wei Zhang

    (Chinese Academy of Sciences)

  • Zhen Fan

    (Chinese Academy of Sciences)

  • Weichao Li

    (Chinese Academy of Sciences)

  • Gong-Li Tang

    (Chinese Academy of Sciences)

  • Youli Xiao

    (Chinese Academy of Sciences
    University of Chinese Academy of Sciences)

  • Guoping Zhao

    (Chinese Academy of Sciences
    University of Chinese Academy of Sciences)

  • Shengying Li

    (Chinese Academy of Sciences
    University of Chinese Academy of Sciences)

Abstract

Rifamycin-derived drugs, including rifampin, rifabutin, rifapentine, and rifaximin, have long been used as first-line therapies for the treatment of tuberculosis and other deadly infections. However, the late steps leading to the biosynthesis of the industrially important rifamycin SV and B remain largely unknown. Here, we characterize a network of reactions underlying the biosynthesis of rifamycin SV, S, L, O, and B. The two-subunit transketolase Rif15 and the cytochrome P450 enzyme Rif16 are found to mediate, respectively, a unique C–O bond formation in rifamycin L and an atypical P450 ester-to-ether transformation from rifamycin L to B. Both reactions showcase interesting chemistries for these two widespread and well-studied enzyme families.

Suggested Citation

  • Feifei Qi & Chao Lei & Fengwei Li & Xingwang Zhang & Jin Wang & Wei Zhang & Zhen Fan & Weichao Li & Gong-Li Tang & Youli Xiao & Guoping Zhao & Shengying Li, 2018. "Deciphering the late steps of rifamycin biosynthesis," Nature Communications, Nature, vol. 9(1), pages 1-9, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-04772-x
    DOI: 10.1038/s41467-018-04772-x
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